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Conserved domains on  [gi|939620385|ref|NP_001303469|]
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uncharacterized protein Dmel_CG11035, isoform B [Drosophila melanogaster]

Protein Classification

J domain-containing protein( domain architecture ID 13425018)

J domain-containing protein similar to Homo sapiens DnaJ homolog subfamily C member 9 (DNAJC9) that acts as a dual histone chaperone and heat shock co-chaperone

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
SCOP:  4000605

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
27-89 4.60e-25

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


:

Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 93.31  E-value: 4.60e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385   27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
25-175 2.59e-04

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG5269:

Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 41.56  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  25 QMSHYDALGI---RRQCTQNEIKAAYYKLSMLYHPDRNQ--GSENAAKKFREINQAYEILGNYRLRRLYDKGI----VHT 95
Cdd:COG5269   42 KVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDfdadVPP 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  96 AGAQYAQDVHDVAEPVVEddAETKFYKSRFQKSRVSDSAGRTPI-------YDFDEWSRNHY--------GKSFDRRQAA 160
Cdd:COG5269  122 PRIYTPDEFFEVWEPVFE--REARFSKKQPVPSLGPSDSSLKEVeefyefwSNFDSWRTFEPldedypddMEERDRKRYS 199
                        170
                 ....*....|....*
gi 939620385 161 QAKyDRIKVQRETNR 175
Cdd:COG5269  200 EAK-NREKRAKLKNQ 213
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
27-89 4.60e-25

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 93.31  E-value: 4.60e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385   27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
28-81 9.49e-22

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 84.52  E-value: 9.49e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGN 81
Cdd:cd06257    2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
28-90 9.31e-21

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 89.88  E-value: 9.31e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNqGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:NF037946   7 YYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDK 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
29-89 5.28e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 87.12  E-value: 5.28e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939620385  29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
26-81 1.04e-19

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 79.59  E-value: 1.04e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 939620385    26 MSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGS-ENAAKKFREINQAYEILGN 81
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSD 57
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
27-91 1.09e-19

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 81.67  E-value: 1.09e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939620385  27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDKG 91
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
29-90 2.36e-18

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 82.26  E-value: 2.36e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939620385   29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
25-175 2.59e-04

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 41.56  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  25 QMSHYDALGI---RRQCTQNEIKAAYYKLSMLYHPDRNQ--GSENAAKKFREINQAYEILGNYRLRRLYDKGI----VHT 95
Cdd:COG5269   42 KVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDfdadVPP 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  96 AGAQYAQDVHDVAEPVVEddAETKFYKSRFQKSRVSDSAGRTPI-------YDFDEWSRNHY--------GKSFDRRQAA 160
Cdd:COG5269  122 PRIYTPDEFFEVWEPVFE--REARFSKKQPVPSLGPSDSSLKEVeefyefwSNFDSWRTFEPldedypddMEERDRKRYS 199
                        170
                 ....*....|....*
gi 939620385 161 QAKyDRIKVQRETNR 175
Cdd:COG5269  200 EAK-NREKRAKLKNQ 213
Cas_III-E_gRAMP NF041225
type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type ...
115-225 7.73e-03

type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type III-E CRISPR/Cas systems, named Cas7-11 because of its multiple domains, works together with the caspase-like TPR-CHAT protease (Csx29) in a subset of type III-E systems. The complex of the Cas7-11 and the TPR-CHAT subunits is called craspase (CRISPR-guided caspase).


Pssm-ID: 469128 [Multi-domain]  Cd Length: 1629  Bit Score: 37.04  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  115 DAETKFYKSRFQKSRVSDSAGRTPIYDFDEWSRNHYGKSFDRRQAAQAKYDRIKVQRETNRISGQtdMVLLAFIFAGVAV 194
Cdd:NF041225  987 SPEHKDYLPDFIPDNGRVIQGGKRIQKESREYRYPFYDRTDTEKLEQEGYERLEAEKIILKNSGR--IKLKDKIKRQELY 1064
                          90       100       110
                  ....*....|....*....|....*....|.
gi 939620385  195 YLMFLAESSYDTPKQKAKERYRRDQEEREQK 225
Cdd:NF041225 1065 KLFALKDKIYKGQKPFTFDLKKKAEKIGRWI 1095
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
27-89 4.60e-25

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 93.31  E-value: 4.60e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385   27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
28-81 9.49e-22

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 84.52  E-value: 9.49e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGN 81
Cdd:cd06257    2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
28-90 9.31e-21

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 89.88  E-value: 9.31e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNqGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:NF037946   7 YYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYDK 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
29-89 5.28e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 87.12  E-value: 5.28e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939620385  29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
26-81 1.04e-19

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 79.59  E-value: 1.04e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 939620385    26 MSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGS-ENAAKKFREINQAYEILGN 81
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSD 57
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
27-91 1.09e-19

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 81.67  E-value: 1.09e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939620385  27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDKG 91
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
29-90 2.36e-18

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 82.26  E-value: 2.36e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939620385   29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
28-90 8.65e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 81.01  E-value: 8.65e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14281   5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
26-90 1.03e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 77.96  E-value: 1.03e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939620385  26 MSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDR 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
28-90 1.21e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 77.92  E-value: 1.21e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14277   7 YYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
28-91 3.36e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 76.24  E-value: 3.36e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNqGSENAAKKFREINQAYEILGNYRLRRLYDKG 91
Cdd:PRK14278   5 YYGLLGVSRNASDAEIKRAYRKLARELHPDVN-PDEEAQEKFKEISVAYEVLSDPEKRRIVDLG 67
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
27-90 6.94e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 75.41  E-value: 6.94e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939620385  27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14286   5 SYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQ 68
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
28-90 1.90e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 74.03  E-value: 1.90e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14294   6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQ 68
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
27-104 3.73e-15

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 68.21  E-value: 3.73e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939620385  27 SHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGS-ENAAKKFREINQAYEILGNYRLRRLYDKGIVHTAGAQYAQDV 104
Cdd:COG2214    6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSASQPS 84
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
28-90 4.73e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 73.27  E-value: 4.73e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSEnAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14291   5 YYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPE-AEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14297 PRK14297
molecular chaperone DnaJ;
28-90 5.21e-15

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 72.89  E-value: 5.21e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14297   6 YYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
29-86 5.96e-15

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 66.95  E-value: 5.96e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 939620385  29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRR 86
Cdd:COG5407    3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
PRK14295 PRK14295
molecular chaperone DnaJ;
28-89 9.26e-15

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 72.19  E-value: 9.26e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:PRK14295  11 YYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
25-99 3.91e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 70.50  E-value: 3.91e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939620385  25 QMSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDKgiVHTAGAQ 99
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINK-EPGAEEKYKEVQEAYETLSDPQKRAAYDQ--YGAAGAN 74
PRK14280 PRK14280
molecular chaperone DnaJ;
28-90 3.96e-14

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 70.52  E-value: 3.96e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14280   6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDINK-EEGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
25-107 4.41e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 70.16  E-value: 4.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  25 QMSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK----GIVHTAGAQY 100
Cdd:PRK14301   3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRfghaGVNGNGGFGG 82

                 ....*..
gi 939620385 101 AQDVHDV 107
Cdd:PRK14301  83 FSSAEDI 89
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
28-96 6.97e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 69.64  E-value: 6.97e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDKgIVHTA 96
Cdd:PRK14285   5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDR-FGHTA 72
PRK14289 PRK14289
molecular chaperone DnaJ;
28-90 1.38e-13

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 69.09  E-value: 1.38e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14289   7 YYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14293 PRK14293
molecular chaperone DnaJ;
29-106 1.57e-13

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 68.86  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQ--GSENaakKFREINQAYEILGNYRLRRLYDK-GIVHTAGAQYAQDVH 105
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKepGAED---RFKEINRAYEVLSDPETRARYDQfGEAGVSGAAGFPDMG 82

                 .
gi 939620385 106 D 106
Cdd:PRK14293  83 D 83
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
28-90 2.22e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 67.66  E-value: 2.22e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14299   6 YYAILGVPKNASQDEIKKAFKKLARKYHPDVNK-SPGAEEKFKEINEAYTVLSDPEKRRIYDT 67
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
28-136 2.54e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 68.28  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRN-QGSENAAKKFREINQAYEILGNYRLRRLYDK-GIV--------HTAG 97
Cdd:PRK14282   6 YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHpENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRfGYVgeqppyqeTESG 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 939620385  98 AQYAQDVHDVAEPVVEDDAETKFYKSRFQKSRVSDSAGR 136
Cdd:PRK14282  86 GGFFEDIFKDFENIFNRDIFDIFFGERRTQEEQREYARR 124
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
28-90 3.10e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 67.95  E-value: 3.10e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14298   7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNK-EPDAEEKFKEISEAYAVLSDAEKRAQYDR 68
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
26-90 4.71e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 67.22  E-value: 4.71e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939620385  26 MSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDR 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
29-107 7.49e-13

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 66.77  E-value: 7.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSEnaakKFREINQAYEILGNYRLRRLYDK----GIVHTAGAQYAQDV 104
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPE----KFKEISRAYEVLSDPEKRKIYDEygeeGLEGGEQPADASDL 106

                 ...
gi 939620385 105 HDV 107
Cdd:PTZ00037 107 FDL 109
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
28-90 2.74e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 65.23  E-value: 2.74e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14283   7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVSE-EEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK14288 PRK14288
molecular chaperone DnaJ;
25-90 1.08e-11

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 63.55  E-value: 1.08e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939620385  25 QMSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDR 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
28-90 1.91e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 62.72  E-value: 1.91e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDrNQGSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14300   5 YYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDR 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
28-90 4.62e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 61.49  E-value: 4.62e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSEN-AAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14290   5 YYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAeAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14279 PRK14279
molecular chaperone DnaJ;
29-89 3.51e-10

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 58.98  E-value: 3.51e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939620385  29 YDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSENAAKKFREINQAYEILGNYRLRRLYD 89
Cdd:PRK14279  12 YKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
28-90 9.74e-10

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 58.26  E-value: 9.74e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385   28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSEnAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PTZ00341  575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKKMYNK 636
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
28-90 1.13e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 57.26  E-value: 1.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14296   6 YYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNK-SPDAHDKMVEINEAADVLLDKDKRKQYDQ 67
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
28-90 5.12e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 55.40  E-value: 5.12e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQgSENAAKKFREINQAYEILGNYRLRRLYDK 90
Cdd:PRK14287   6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDVNK-APDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
24-83 7.42e-09

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 50.95  E-value: 7.42e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939620385  24 HQMSHYDALGIRRQCTQNEIKAAYYKLSMLYHPDR--NQGSE----NAAKKFREINQAYEILGNYR 83
Cdd:COG1076    2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEeeqrLALQKAAAINEAYETLKDPR 67
PRK10266 PRK10266
curved DNA-binding protein;
28-105 5.98e-07

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 49.05  E-value: 5.98e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939620385  28 HYDALGIRRQCTQNEIKAAYYKLSMLYHPDRNQGSeNAAKKFREINQAYEILGNYRLRRLYDKGIVHTAGAQYAQDVH 105
Cdd:PRK10266   6 YYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEP-DAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQFQ 82
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
25-175 2.59e-04

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 41.56  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  25 QMSHYDALGI---RRQCTQNEIKAAYYKLSMLYHPDRNQ--GSENAAKKFREINQAYEILGNYRLRRLYDKGI----VHT 95
Cdd:COG5269   42 KVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDfdadVPP 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  96 AGAQYAQDVHDVAEPVVEddAETKFYKSRFQKSRVSDSAGRTPI-------YDFDEWSRNHY--------GKSFDRRQAA 160
Cdd:COG5269  122 PRIYTPDEFFEVWEPVFE--REARFSKKQPVPSLGPSDSSLKEVeefyefwSNFDSWRTFEPldedypddMEERDRKRYS 199
                        170
                 ....*....|....*
gi 939620385 161 QAKyDRIKVQRETNR 175
Cdd:COG5269  200 EAK-NREKRAKLKNQ 213
djlA PRK09430
co-chaperone DjlA;
21-79 2.40e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 38.25  E-value: 2.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939620385  21 SQRHQMSH-YDALGIRRQCTQNEIKAAYYKLSMLYHPDR--NQG-----SENAAKKFREINQAYEIL 79
Cdd:PRK09430 194 QRGPTLEDaYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvAKGlppemMEMAKEKAQEIQAAYELI 260
Cas_III-E_gRAMP NF041225
type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type ...
115-225 7.73e-03

type III-E CRISPR-associated gRAMP effector Cas7-11; The giant RAMP (gRAMP) effector of type III-E CRISPR/Cas systems, named Cas7-11 because of its multiple domains, works together with the caspase-like TPR-CHAT protease (Csx29) in a subset of type III-E systems. The complex of the Cas7-11 and the TPR-CHAT subunits is called craspase (CRISPR-guided caspase).


Pssm-ID: 469128 [Multi-domain]  Cd Length: 1629  Bit Score: 37.04  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939620385  115 DAETKFYKSRFQKSRVSDSAGRTPIYDFDEWSRNHYGKSFDRRQAAQAKYDRIKVQRETNRISGQtdMVLLAFIFAGVAV 194
Cdd:NF041225  987 SPEHKDYLPDFIPDNGRVIQGGKRIQKESREYRYPFYDRTDTEKLEQEGYERLEAEKIILKNSGR--IKLKDKIKRQELY 1064
                          90       100       110
                  ....*....|....*....|....*....|.
gi 939620385  195 YLMFLAESSYDTPKQKAKERYRRDQEEREQK 225
Cdd:NF041225 1065 KLFALKDKIYKGQKPFTFDLKKKAEKIGRWI 1095
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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